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Cellobiose dehydrogenase
Summary
- UniProt ID
- A9XK88
- Gene Symbol
-
- CDH
- Organism
- Thermothelomyces myriococcoides
External Links
- Re-Glyco
- A9XK88
Annotation
- Keyword
-
- 3D-structure
- FAD
- Heme
- Nucleotide-binding
- Oxidoreductase
- Polysaccharide degradation
- Pyrrolidone carboxylic acid
- Signal
- Gene Ontology (GO)
| GO Term |
|---|
| extracellular region |
| GO Term |
|---|
| polysaccharide catabolic process |
| GO Term |
|---|
| oxidoreductase activity, acting on CH-OH group of donors |
| metal ion binding |
| cellulose binding |
| flavin adenine dinucleotide binding |
Sequence
MRTSSRLIGALAAALLPSALAQNNVPNTFTDPDSGITFNTWGLDEDSPQTQGGFTFGVALPSDALTTDASEFIGYLKCARNDESGWCGISLGGPMTNSLLITAWPHEDTVYTSLRFATGYAMPDVYEGDAEITQVSSSVNSTHFSLIFRCKNCLQWSHGGSSGGASTSGGVLVLGWVQAFDDPGNPTCPEQITLQQHDNGMGIWGAQLNTDAASPSYTDWAAQATKTVTGDCEGPTETSVVGVPVPTGVSFDYIVVGGGAGGIPAADKLSEAGKSVLLIEKGFASTANTGGTLGPEWLEGHDLTRFDVPGLCNQIWVDSKGIACEDTDQMAGCVLGGGTAVNAGLWFKPYSLDWDYLFPDGWKYNDVQPAINRALSRIPGTDAPSTDGKRYYQEGFEVLSKGLAAGGWTSVTANNAPDKKNRTFAHAPFMFAGGERNGPLGTYFQTAKKRNNFDVWLNTSVKRVIREGGHITGVEVEPFRDGGYEGIVPVTKVTGRVILSAGTFGSAKILLRSGIGPEDQLEVVAASEKDGPTMIGNSSWINLPVGYNLDDHLNTDTVISHPDVVFYDFYEAWDDPIESDKNSYLESRTGILAQAAPNIGPMFWEEIVGADGIVRQLQWTARVEGSLGAPNGHTMTMSQYLGRGATSRGRMTITPSLTTIVSDVPYLKDPNDKEAVIQGIINLQNALQNVANLTWLFPNSTITPREYVESMVVSPSNRRSNHWMGTNKLGTDDGRKGGSAVVDLDTRVYGTDNLFVIDASIFPGVPTTNPTSYIVVAAEHASSRILALPDLEPVPKYGQCGGREWTGSFVCADGSTCEYQNEWYSQCL
Glycosylation Sites
| Position | Description | PubMed ID | GlyTouCan ID | Source |
|---|---|---|---|---|
| 140 | N-linked (GlcNAc...) asparagine |
|
||
| 216 | O-linked (Man...) threonine |
|
||
| 218 | O-linked (Man...) threonine |
|
||
| 225 | O-linked (Man...) threonine |
|
||
| 227 | O-linked (Man...) threonine |
|
||
| 247 | O-linked (Man...) threonine |
|
||
| 421 | N-linked (GlcNAc...) asparagine |
|
||
| 458 | N-linked (GlcNAc...) asparagine |
|
||
| 537 | N-linked (GlcNAc...) asparagine |
|
||
| 699 | N-linked (GlcNAc...) asparagine |
|
Feature
: Glycosylation Site from GlyGen
: Glycosylation Site from UniProt
